The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
SPIN-STATE CHANGES IN CYTOCHROME P-450 cam ON BINDING OF SPECIFIC SUBSTRATES
Open accessAbstract
The electron paramagnetic resonance signals of the soluble P-450 cytochrome from Pseudomonas putida were observed at temperatures from 4.2 to 80°K. As isolated, P-450 has a signal typical of a low spin ferric-heme compound with sulfur as one of the axial ligands ( g = 2.45, 2.26, 1.91 5 ). We also detected a minor signal typical of high spin ferric heme ( g = 8, 4, 1.8) equivalent to less than 7% of the heme at temperatures below 20°K. On titration with the substrate, (+)-camphor, the low spin signal decreased and the high spin signal increased, maximally representing about 60% of the heme. For reasons not thus far understood, 40% of the heme is not converted to high spin by either (+) or (-)-camphor. The high spin signal has a rhombic character which is stronger than any previously observed with a heme compound ( E = 0.33 cm -1 ; D = 3.8 cm -1 ; E / D = 0.087). We conclude that P-450 cam as isolated is equal to or more than 95% in a low spin form probably having sulfur as one of the axial ligands. The binding of substrate displaces this ligand sufficiently to allow for conversion from a low to a high spin form.
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Cites
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Klingenberg, M. (1958) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(58)90436-3 · Cited by 664
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Self-citationGarfinkel, D. (1958) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(58)90095-x · Cited by 437
Pigments of rat liver microsomes
Klingenberg, M. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00621-5 · Cited by 411
Drug Interaction with Hepatic Microsomal Cytochrome
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Cited by
Structure and chemistry of cytochrome p450
Denisov, I. G., Makris, T. M., Sligar, S. G., & Schlichting, I. (2005) · Chemical Reviews · doi:10.1021/cr0307143 · Cited by 2,106
Theoretical Perspective on the Structure and Mechanism of Cytochrome P450 Enzymes
Shaik, S., Kumar, D., de Visser, S. P., Altun, A., & Thiel, W. (2005) · Chemical Reviews · doi:10.1021/cr030722j · Cited by 1,236
P450 Enzymes: Their Structure, Reactivity, and Selectivity—Modeled by QM/MM Calculations
Shaik, S., Cohen, S., Wang, Y., Chen, H., Kumar, D., & Thiel, W. (2010) · Chemical Reviews · doi:10.1021/cr900121s · Cited by 1,083
Probing Structure-Function Relations in Heme-Containing Oxygenases and Peroxidases
Dawson, J. H. (1988) · Science · doi:10.1126/science.3358128 · Cited by 929
Stuehr, D. J., & Ikeda-Saito, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36718-3 · Cited by 347
Metadata
- Authors
- Tsai, R., Yu, C. A., Gunsalus, I. C., Peisach, J., Blumberg, W., Orme-Johnson, W. H., & Beinert, H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1970-08
- Volume
- 66
- Issue
- 4
- Pages
- 1157-1163
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1985856334
- Cited by
- 270
- References
- 9
- FWCI
- 21.90
- Type
- journal article
- Language
- en
- Open access
- green
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- Tsai, R., Yu, C. A., Gunsalus, I. C., Peisach, J., Blumberg, W., Orme-Johnson, W. H., & Beinert, H. (1970). SPIN-STATE CHANGES IN CYTOCHROME P-450 cam ON BINDING OF SPECIFIC SUBSTRATES. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.66.4.1157
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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